水热法提取丝胶蛋白的理化性质研究

IF 1.4 4区 生物学 Q4 BIOCHEMISTRY & MOLECULAR BIOLOGY
I. Sh. Goyibnazarov, S. S. Yarmatov, B. J. Kholturayev, Kh. O. Eshchanov, I. B. Sapaev, Sh. A. Yuldoshov, A. A. Sarymsakov, Kh. S. Toshov
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引用次数: 0

摘要

在这项工作中,研究了在不使用化学试剂的情况下,在100°C和110°C的温度下,在2-24 h的时间内,从蚕茧中完全提取蚕丝蛋白。得到分子量在20 ~ 240 kDa之间的丝胶蛋白样品。在热干燥和升华干燥分离丝胶样品,观察其溶解度的变化。利用x射线衍射(XRD)和傅里叶变换红外光谱(FTIR)分析了热干燥丝胶样品的结构变化。XRD分析发现,样品的衍射峰位于18.9°和20.7°,表明存在结晶结构,而经升华干燥的样品则表现为完全无定形结构。FTIR光谱显示,热干燥样品在3000 ~ 3500cm -1和1500 ~ 1600cm -1波段展宽,这是由于与升华干燥样品相比,形成了大量的氢键。流变学分析进一步表明,丝胶蛋白样品的损失模量大于储存模量。结果表明,高温下无化学试剂提取丝胶可有效分离不同分子量的丝胶蛋白,而干燥方法对丝胶蛋白的结构、溶解度和流变性能影响较大。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Physico-Chemical Properties of Silk Sericin Extracted by Hydrothermal Treatment

In this work, studies were conducted to achieve the complete extraction of sericin from natural silk cocoons at temperatures of 100 °C and 110 °C for durations ranging 2–24 h without the use of chemical reagents. As a result, sericin samples with molecular weight changing 20–240 kDa were obtained. During the thermal and sublimation drying of the isolated sericin samples, changes in their solubility were observed. Structural changes in the thermally dried sericin samples were analyzed using X-ray diffraction (XRD) and Fourier transform infrared (FTIR) spectroscopy. XRD analysis revealed diffraction peaks at 18.9° and 20.7°, indicating the presence of crystalline structure, whereas the samples dried by sublimation exhibited a completely amorphous structure. FTIR spectroscopy showed band broadening in the regions of 3000–3500 cm− 1 and 1500–1600 cm− 1 in the thermally dried samples, which was attributed to extensive hydrogen-bond formation compared to the samples dried by sublimation. Rheological analysis further demonstrated that the loss modulus exceeded the storage modulus for sericin sample. The results demonstrate that extract sericin under high temperature without chemical reagent enables the efficient isolation of sericin with different molecular weight, while the drying method strongly influences its structural, solubility, and rheological properties.

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来源期刊
The Protein Journal
The Protein Journal 生物-生化与分子生物学
CiteScore
5.20
自引率
0.00%
发文量
57
审稿时长
12 months
期刊介绍: The Protein Journal (formerly the Journal of Protein Chemistry) publishes original research work on all aspects of proteins and peptides. These include studies concerned with covalent or three-dimensional structure determination (X-ray, NMR, cryoEM, EPR/ESR, optical methods, etc.), computational aspects of protein structure and function, protein folding and misfolding, assembly, genetics, evolution, proteomics, molecular biology, protein engineering, protein nanotechnology, protein purification and analysis and peptide synthesis, as well as the elucidation and interpretation of the molecular bases of biological activities of proteins and peptides. We accept original research papers, reviews, mini-reviews, hypotheses, opinion papers, and letters to the editor.
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